The mechanism of auxin-enhanced synthesis of RNA by chromatin is under study. Investigations will concentrate on 1) comparative analyses of chromatin-associated RNA polymerases from control and auxin-treated tissues, and 2) parallel comparative studies on chromatin proteins, empahsizing modifications (e.g. phosphorylation, acetylation, etc.) of existing chromatin proteins in addition to synthesis-turnover studies of the acidic or non-histone protein complement. The in vivo level of enhancement of RNA synthesis (greater than 5- fold for rRNA) is expressed in chromatin (operationally chromatin I) isolated from auxin-treated tissue. Further crude solubilized RNA polymerase activity from the chromatin is 5 to 10 fold greater from auxin chromatin I. RNA polymerase I represents greater than 95% of chromatin I-associated RNA polymerase activity. The enzyme from control and auxin chromatin will be purified to homogeneity in order to assess if there is more of the same enzyme, a modified enzyme of greater specific activity, or a regulatory factor in the crude solubilized enzyme which separates during purification and which accounts for the greater enzyme activity. Similar studies will be done with RNA polymerase II.